2W1T

Crystal Structure of B. subtilis SpoVT

Summary for 2W1T

• Entry DOI: 10.2210/pdb2w1t/pdb
• Related: 2W1R
• Descriptor: STAGE V SPORULATION PROTEIN T (3 entities in total)
• Functional Keywords: transcription, transcription regulation, repressor, activator, sporulation, dna-binding, gaf domain regulated tetrameric spovt
• Biological source: BACILLUS SUBTILIS; More
• Total number of polymer chains: 2
• Total formula weight: 39520.84

Authors

Asen, I.,Djuranovic, S.,Lupas, A.N.,Zeth, K. (deposition date: 2008-10-20, release date: 2008-11-18, Last modification date: 2024-05-08)

Primary citation

Asen, I.,Djuranovic, S.,Lupas, A.N.,Zeth, K.
Crystal Structure of Spovt, the Final Modulator of Gene Expression During Spore Development in Bacillus Subtilis
J.Mol.Biol., 386:962-, 2009

PubMed Abstract: Endospore formation in Bacillus subtilis is orchestrated by five developmental sigma factors and further modulated by several auxiliary transcription factors. One of these, SpoVT, regulates forespore-specific sigma(G)-dependent genes and plays a key role in the final stages of spore formation. We have determined the crystal structure of the isolated C-terminal domain of SpoVT at 1.5 A by experimental phasing techniques and used this model to solve the structure of the full-length SpoVT at 2.6 A by molecular replacement. SpoVT is a tetramer that shows an overall significant distortion mediated by electrostatic interactions. Two monomers dimerize via the highly charged N-terminal domains to form swapped-hairpin beta-barrels. These asymmetric dimers further tetramerize through the formation of mixed helix bundles between their C-terminal domains, which themselves fold as GAF (cGMP-specific and cGMP-stimulated phosphodiesterases, Anabaena adenylate cyclases, and Escherichia coli FhlA) domains. The combination of a swapped-hairpin beta-barrel with a GAF domain represents a novel domain architecture in transcription factors. The occurrence of SpoVT homologs throughout Bacilli and Clostridia demonstrates the ancestral origin of this factor in sporulation.

PubMed: 18996130
DOI: 10.1016/J.JMB.2008.10.061

Experimental method

X-RAY DIFFRACTION (2.6 Å)